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Journal articles on the topic 'Osteoponten'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Chiu, Tai-Jan, Hung-I. Lu, Chang-Han Chen, et al. "Osteopontin Expression Is Associated with the Poor Prognosis in Patients with Locally Advanced Esophageal Squamous Cell Carcinoma Receiving Preoperative Chemoradiotherapy." BioMed Research International 2018 (2018): 1–9. http://dx.doi.org/10.1155/2018/9098215.

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Background. The osteopontin has been involved in therapeutic resistance in a variety of cancers. But, the significance of osteopontin expression on the prognosis of patients with locally advanced esophageal squamous cell carcinoma (ESCC) receiving chemoradiotherapy is unclear.Methods.In 80 patients with locally advanced ESCC receiving preoperative chemoradiotherapy between 1999 and 2012, osteopontin expression was evaluated by immunohistochemistry and correlated with treatment outcome. The functional role of osteopontin in ESCC cell lines was determined by osteopontin-mediated siRNA.Results. O

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2

Sodek, J., B. Ganss, and M. D. McKee. "Osteopontin." Critical Reviews in Oral Biology & Medicine 11, no. 3 (2000): 279–303. http://dx.doi.org/10.1177/10454411000110030101.

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Osteopontin (OPN) is a highly phosphorylated sialoprotein that is a prominent component of the mineralized extracellular matrices of bones and teeth. OPN is characterized by the presence of a polyaspartic acid sequence and sites of Ser/Thr phosphorylation that mediate hydroxyapatite binding, and a highly conserved RGD motif that mediates cell attachment/signaling. Expression of OPN in a variety of tissues indicates a multiplicity of functions that involve one or more of these conserved motifs. While the lack of a clear phenotype in OPN "knockout" mice has not established a definitive role for

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3

Scatena, Marta, Lucy Liaw, and Cecilia M. Giachelli. "Osteopontin." Arteriosclerosis, Thrombosis, and Vascular Biology 27, no. 11 (2007): 2302–9. http://dx.doi.org/10.1161/atvbaha.107.144824.

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4

Szalay, Gudrun, Martina Sauter, Michael Haberland, et al. "Osteopontin." Circulation Research 104, no. 7 (2009): 851–59. http://dx.doi.org/10.1161/circresaha.109.193805.

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5

Shaheen, Mazen, and Neal L. Weintraub. "Osteopontin." Arteriosclerosis, Thrombosis, and Vascular Biology 27, no. 3 (2007): 439–41. http://dx.doi.org/10.1161/01.atv.0000258640.30287.7b.

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6

Demer, Linda L., and Yin Tintut. "Osteopontin." Circulation Research 84, no. 2 (1999): 250–52. http://dx.doi.org/10.1161/01.res.84.2.250.

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7

Chellaiah, M. A., and K. A. Hruska. "Osteopontin." Drug News & Perspectives 11, no. 6 (1998): 350. http://dx.doi.org/10.1358/dnp.1998.11.6.863656.

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8

Vogt, Mario HJ, Joop ten Kate, Roosmarie JM Drent, Chris H. Polman, and Raymond Hupperts. "Increased osteopontin plasma levels in multiple sclerosis patients correlate with bone-specific markers." Multiple Sclerosis Journal 16, no. 4 (2010): 443–49. http://dx.doi.org/10.1177/1352458509359723.

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The pro-inflammatory cytokine osteopontin has been found to be highly expressed in multiple sclerosis lesions and plasma levels are increased during relapses in relapse-onset multiple sclerosis patients. The objective was to determine the relationship between osteopontin plasma and cerebrospinal fluid levels in relation to the immunoglobulin G index. In addition, osteopontin plasma levels were compared with osteopontin mRNA levels in peripheral blood mononuclear cells and bone-specific markers to analyse whether osteopontin may be peripherally produced. Osteopontin and bone-specific markers we

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9

Feldreich, Tobias, Axel C. Carlsson, Johanna Helmersson-Karlqvist, et al. "Urinary Osteopontin Predicts Incident Chronic Kidney Disease, while Plasma Osteopontin Predicts Cardiovascular Death in Elderly Men." Cardiorenal Medicine 7, no. 3 (2017): 245–54. http://dx.doi.org/10.1159/000476001.

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Background and Objectives: The matricellular protein osteopontin is involved in the pathogenesis of both kidney and cardiovascular disease. However, whether circulating and urinary osteopontin levels are associated with the risk of these diseases is less studied. Design, Setting, Participants, and Measurements: A community-based cohort of elderly men (Uppsala Longitudinal Study of Adult Men [ULSAM]; n = 741; mean age: 77 years) was used to study the associations between plasma and urinary osteopontin, incident chronic kidney disease, and the risk of cardiovascular death during a median of 8 ye

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10

Merry, K., R. Dodds, A. Littlewood, and M. Gowen. "Expression of osteopontin mRNA by osteoclasts and osteoblasts in modelling adult human bone." Journal of Cell Science 104, no. 4 (1993): 1013–20. http://dx.doi.org/10.1242/jcs.104.4.1013.

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Over recent years several non-collagenous matrix proteins of bone have been isolated and characterized. One of these proteins, osteopontin, has been shown to be synthesized by osteoblasts and deposited in the bone matrix where it is thought to bind to hydroxyapatite. However much of the functional evidence is circumstantial, and the precise function of osteopontin has not been fully elucidated. We have used in situ hybridization techniques to investigate the expression of osteopontin mRNA in a variety of human bone tissues. Cryostat sections of human osteophyte and osteoclastoma tissue were hy

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Berman, Jeffrey S., David Serlin, Xinfang Li, et al. "Altered bleomycin-induced lung fibrosis in osteopontin-deficient mice." American Journal of Physiology-Lung Cellular and Molecular Physiology 286, no. 6 (2004): L1311—L1318. http://dx.doi.org/10.1152/ajplung.00394.2003.

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Osteopontin is a multifunctional matricellular protein abundantly expressed during inflammation and repair. Osteopontin deficiency is associated with abnormal wound repair characterized by aberrant collagen fibrillogenesis in the heart and skin. Recent gene microarray studies found that osteopontin is abundantly expressed in both human and mouse lung fibrosis. Macrophages and T cells are known to be major sources of osteopontin. During lung fibrosis, however, osteopontin expression continues to increase when inflammation has receded, suggesting alternative sources of ostepontin during this res

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12

Brown, L. F., B. Berse, L. Van de Water, et al. "Expression and distribution of osteopontin in human tissues: widespread association with luminal epithelial surfaces." Molecular Biology of the Cell 3, no. 10 (1992): 1169–80. http://dx.doi.org/10.1091/mbc.3.10.1169.

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Osteopontin, a glycoprotein with a glycine-arginine-glycine-aspartate-serine (GRGDS) cell-binding domain, has been described in bone and is also known to be expressed in other organs, particularly kidney. The goal of the present work was to define the distribution of osteopontin synthesis and deposition in a wide variety of normal adult human tissues using a multifaceted approach that included immunohistochemistry, in situ hybridization, and Northern analysis. Immunohistochemical studies have revealed the unexpected finding that osteopontin is deposited as a prominent layer at the luminal surf

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13

HUDKINS, KELLY L., CECILIA M. GIACHELLI, YAN CUI, WILLIAM G. COUSER, RICHARD J. JOHNSON, and CHARLES E. ALPERS. "Osteopontin Expression in Fetal and Mature Human Kidney." Journal of the American Society of Nephrology 10, no. 3 (1999): 444–57. http://dx.doi.org/10.1681/asn.v103444.

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Abstract. Osteopontin is a secreted phosphoprotein that is expressed by normal kidney, and has been associated with a number of functions including cell adhesion, migration, signaling, and biomineralization. Although there is a vast literature detailing osteopontin localization in various rodent models of both development and disease, this article presents the first comprehensive description of osteopontin localization in human kidney. In this study, immunohistochemistry, immunoelectron microscopy,in situhybridization, and Northern blotting are used to analyze osteopontin protein and mRNA expr

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14

Marques, Durval Santos, Jessica Grativol, Rodrigo Alves da Silva Peres, Aline da Rocha Matos, and Etel Rodrigues Pereira Gimba. "Osteopontin-c isoform levels are associated with SR and hnRNP differential expression in ovarian cancer cell lines." Tumor Biology 39, no. 9 (2017): 101042831772544. http://dx.doi.org/10.1177/1010428317725442.

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Osteopontin-c splicing isoform activates ovarian cancer progression features. Imbalanced expression of splicing factors from serine/arginine -rich and heterogeneous ribonucleoproteins families has been correlated with the generation of oncogenic splicing isoforms. Our goal was to investigate whether there is any association between the transcriptional patterns of these splicing factors in ovarian cells and osteopontin-c expression levels. We also aimed to investigate the occurrence of these splicing factors binding sites inside osteopontin exon 4 and adjacent introns. To test associations betw

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Lamort, Anne-Sophie, Ioanna Giopanou, Ioannis Psallidas, and Georgios T. Stathopoulos. "Osteopontin as a Link between Inflammation and Cancer: The Thorax in the Spotlight." Cells 8, no. 8 (2019): 815. http://dx.doi.org/10.3390/cells8080815.

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The glycoprotein osteopontin (OPN) possesses multiple functions in health and disease. To this end, osteopontin has beneficial roles in wound healing, bone homeostasis, and extracellular matrix (ECM) function. On the contrary, osteopontin can be deleterious for the human body during disease. Indeed, osteopontin is a cardinal mediator of tumor-associated inflammation and facilitates metastasis. The purpose of this review is to highlight the importance of osteopontin in malignant processes, focusing on lung and pleural tumors as examples.

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Bayless, K. J., G. A. Meininger, J. M. Scholtz, and G. E. Davis. "Osteopontin is a ligand for the alpha4beta1 integrin." Journal of Cell Science 111, no. 9 (1998): 1165–74. http://dx.doi.org/10.1242/jcs.111.9.1165.

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Recent work has shown that osteopontin expression is upregulated at sites of cardiovascular injury. It has been hypothesized that osteopontin provides an adhesive matrix for endothelial and smooth muscle cells during remodeling of the vascular wall following injury. Osteopontin has also been found to be synthesized by monocytes and macrophages within injury sites. Here, we present data showing that osteopontin can promote leukocyte adhesion through the alpha4beta1 integrin. In the presence of physiologic concentrations of Mg2+ and Ca2+, osteopontin purified from bovine milk promoted cell-subst

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Hong, Qu, Lawrence F. Brown, Harold F. Dvorak, and Ann M. Dvorak. "Ultrastructural Immunogold Localization of Osteopontin in Human Gastric Mucosa." Journal of Histochemistry & Cytochemistry 45, no. 1 (1997): 21–33. http://dx.doi.org/10.1177/002215549704500104.

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We performed ultrastructural immunogold localization of osteopontin in the mucosa of human stomach. This adhesive glycoprotein was present in mucous and chief cells of the epithelial layer and in macrophages in the lamina propria. Parietal and endocrine cells of the epithelial layer and mast cells and plasma cells in the lamina propria did not contain osteopontin, serving as internal negative controls. Subcellular localizations of osteopontin included secretory granules and synthetic organelles in mucous and chief cells and phagolysosomes in macrophages. Extracellular concentrations of osteopo

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18

Loosen, Sven, Daniel Heise, Cees Dejong, et al. "Circulating Levels of Osteopontin Predict Patients’ Outcome after Resection of Colorectal Liver Metastases." Journal of Clinical Medicine 7, no. 11 (2018): 390. http://dx.doi.org/10.3390/jcm7110390.

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For colorectal liver metastases (CRLM), surgical resection is the only potentially curative therapy, but even successfully resected patients often face disease recurrence, leading to 5-year survival rate below 50%. Despite available preoperative stratification strategies, it is not fully elucidated which patients actually benefit from CRLM resection. Here we evaluated osteopontin, a secreted glyco-phosphoprotein, as a biomarker in the context of CRLM resection. Tissue levels of osteopontin were analysed in CRLM using reverse transcription polymerase chain reaction (RT-PCR) and immunohistochemi

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19

Pilli, Ganga S., Prakash V. Patil, and SG Karadesai. "Osteopontin as a Prognostic Indicator in Grading of Ovarian Epithelial Tumors." Journal of South Asian Federation of Obstetrics and Gynaecology 7, no. 2 (2015): 61–63. http://dx.doi.org/10.5005/jp-journals-10006-1324.

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ABSTRACT Aim To determine if osteopontin expression by immunohistochemistry (IHC) can correlate with histological type and grade of epithelial ovarian cancer. Materials and methods The present work has been carried out at department of pathology, of a reputed medical college in Belgaum district of Karnataka state. The study is carried out for a period of 18 months for data collection, evaluation of the marker and data analysis. All consecutive specimens of ovarian tumors are included in the study. The study included 55 epithelial ovarian tumors and these are analyzed histopathologically. In al

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Choi, Steve S., Lee C. Claridge, Ravi Jhaveri, et al. "Osteopontin is up-regulated in chronic hepatitis C and is associated with cellular permissiveness for hepatitis C virus replication." Clinical Science 126, no. 12 (2014): 845–55. http://dx.doi.org/10.1042/cs20130473.

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Osteopontin is up-regulated in patients with chronic hepatitis C, and directly promotes hepatitis C replication. Reducing osteopontin represses hepatitis C levels. Serum osteopontin levels correlate with disease severity and may predict response to anti-viral treatment.

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Angelucci, Adriano, Claudio Festuccia, Gabriele DAndrea, Anna Teti, and Mauro Bologna. "Osteopontin Modulates Prostate Carcinoma Invasive Capacity through RGD-Dependent Upregulation of Plasminogen Activators." Biological Chemistry 383, no. 1 (2002): 229–34. http://dx.doi.org/10.1515/bc.2002.024.

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Abstract Osteopontin, a noncollageneous bone matrix protein, is produced in several human tumors but its role in cancer progression has been only partially elucidated. In this study we investigated the potential role of osteopontin in the malignancy of prostate cancer cells. Chemotaxis and chemoinvasion analyses revealed a dosedependent increase in PC3 cell movement induced by osteopontin and a strict dependence of cell invasion on αvβ3 integrin function. The pattern of protease expression was modified by osteopontin and was characterized by an upregulation of plasminogen activators. Our findi

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22

Hotte, Sebastien J., Eric W. Winquist, Larry Stitt, Sylvia M. Wilson, and Ann F. Chambers. "Plasma osteopontin." Cancer 95, no. 3 (2002): 506–12. http://dx.doi.org/10.1002/cncr.10709.

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23

RODAN, GIDEON A. "Osteopontin Overview." Annals of the New York Academy of Sciences 760, no. 1 Osteopontin (1995): 1–5. http://dx.doi.org/10.1111/j.1749-6632.1995.tb44614.x.

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Pero, M. E., G. J. Killian, P. Lombardi, L. Zicarelli, L. Avallone, and B. Gasparrini. "327 IDENTIFICATION OF OSTEOPONTIN IN WATER BUFFALO SEMEN." Reproduction, Fertility and Development 19, no. 1 (2007): 279. http://dx.doi.org/10.1071/rdv19n1ab327.

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The competitiveness of buffalo breeding will depend on the utilization of reproductive biotechnologies that allows acceleration of genetic progress. A major factor hampering the efficiency of both artificial insemination and in vitro embryo production programs in this species is male hypofertility. Reports for several species suggest that seminal plasma contains factors that influence male fertility. Osteopontin is a glycoprotein found in several biological fluids including seminal plasma, and its presence is associated with spermatozoa concentration. In cattle, expression of osteopontin was h

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Coombes, Jason D., and Wing-Kin Syn. "Differential osteopontin functions: The role of osteopontin isoforms." Hepatology 62, no. 1 (2015): 323–24. http://dx.doi.org/10.1002/hep.27555.

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Abd El Dayem, Soha M., Abo El Magd El Bohy, Ahmed A. Battah, Mona Hamed, and Shereen Hamdy Abd El Aziz. "Osteopontin for Early Detection of Microvascular and Macrovascular Type 1 Diabetic Complication." Open Access Macedonian Journal of Medical Sciences 7, no. 21 (2019): 3619–22. http://dx.doi.org/10.3889/oamjms.2019.613.

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AIM: To evaluate the relationship between osteopontin and diabetes complication in type 1 diabetic patient. PATIENTS AND METHODS: Seventy types 1 diabetic and 60 healthy volunteers were studied. Full history, examination, laboratory tests of glycosylated haemoglobin (HbA1c), serum lipids {cholesterol, triglyceride (Tg), high-density lipoprotein-cholesterol (HDL-c), low-density lipoprotein – cholesterol (LDL-c)}, oxidised low-density lipoprotein (OxLDL), Osteopontin and urinary microalbuminuria (albumin/creatinine ratio) were done. Image study in the form of a carotid intimal medial thick

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Rogers, S. A., B. J. Padanilam, K. A. Hruska, C. M. Giachelli, and M. R. Hammerman. "Metanephric osteopontin regulates nephrogenesis in vitro." American Journal of Physiology-Renal Physiology 272, no. 4 (1997): F469—F476. http://dx.doi.org/10.1152/ajprenal.1997.272.4.f469.

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Renal expression of osteopontin is enhanced in the setting of acute ischemic injury. Because of the parallels that exist between recovery from renal ischemia and renal development, we characterized the role that osteopontin plays during metanephrogenesis in the rat. Osteopontin mRNA is present in kidneys obtained from rat embryos as early as embryonic day 13 (E13). Immunohistochemical staining of metanephroi obtained from E16 rat embryos and metanephroi obtained from E13 embryos and cultured for 3 days in vitro demonstrated that osteopontin is expressed both in the developing nephron and in th

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Crivello, Joseph F., and E. Delvin. "Isolation and characterization of a cDNA for osteopontin-k: A kidney cell adhesion molecule with high homology to osteopontins." Journal of Bone and Mineral Research 7, no. 6 (2009): 693–99. http://dx.doi.org/10.1002/jbmr.5650070614.

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Choi, K. W., D. W. Kim, and S. W. Lee. "Purification and Properties of Osteopontin from Bovine Milk." Journal of Animal Science and Technology 45, no. 3 (2003): 491–98. http://dx.doi.org/10.5187/jast.2003.45.3.491.

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Madsen, K. M., L. Zhang, A. R. Abu Shamat, S. Siegfried, and J. H. Cha. "Ultrastructural localization of osteopontin in the kidney: induction by lipopolysaccharide." Journal of the American Society of Nephrology 8, no. 7 (1997): 1043–53. http://dx.doi.org/10.1681/asn.v871043.

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Osteopontin is a secreted phosphoprotein that is expressed in the normal kidney and induced during various pathologic conditions associated with tubulointerstitial injury. However, the exact cellular location of osteopontin in the kidney has been a matter of controversy, and little is known about the role of osteopontin in the kidney. The purpose of this study was to establish the cellular and intracellular distribution of osteopontin in the rat kidney under normal conditions and after injection of a bacterial endotoxin lipopolysaccharide (LPS). Animals received injections of LPS or vehicle at

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Chellaiah, M., and K. Hruska. "Osteopontin stimulates gelsolin-associated phosphoinositide levels and phosphatidylinositol triphosphate-hydroxyl kinase." Molecular Biology of the Cell 7, no. 5 (1996): 743–53. http://dx.doi.org/10.1091/mbc.7.5.743.

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Based on previous studies demonstrating activation of phosphatidylinositol 3-hydroxyl kinase (PI3-kinase) and stimulation of a change in cell shape, we examined the effect of osteopontin on the association of phospholipids with gelsolin, an actin-capping/severing protein. Osteopontin stimulated a rapid increase in phosphatidylinositol bisphosphate and phosphatidylinositol triphosphate levels associated with gelsolin in Triton-soluble fractions of cell lysates. The increased levels of phosphatidylinositol triphosphate associated with gelsolin were due to stimulation of PI3-kinase activity assoc

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Larsson, Anders, Johanna Helmersson-Karlqvist, Lars Lind, Johan Ärnlöv, and Tobias Rudholm Feldreich. "Strong Associations between Plasma Osteopontin and Several Inflammatory Chemokines, Cytokines, and Growth Factors." Biomedicines 9, no. 8 (2021): 908. http://dx.doi.org/10.3390/biomedicines9080908.

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Osteopontin is a member of the proinflammatory cytokine network, a complex system that involves many chemokines, cytokines, and growth factors. The aim of the present study was to study the associations between osteopontin and a large number of chemokines, cytokines, and growth factors. We analyzed plasma and urine osteopontin in 652 men from the Uppsala Longitudinal Study of Adult Men (ULSAM) study cohort and compared the levels with the levels of eighty-five chemokines, cytokines, and growth factors. We found significant associations between plasma osteopontin and 37 plasma biomarkers in a m

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Maniatis, Konstantinos, Gerasimos Siasos, Evangelos Oikonomou, et al. "Osteoprotegerin and Osteopontin Serum Levels are Associated with Vascular Function and Inflammation in Coronary Artery Disease Patients." Current Vascular Pharmacology 18, no. 5 (2020): 523–30. http://dx.doi.org/10.2174/1570161117666191022095246.

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Background: Osteoprotegerin and osteopontin have recently emerged as key factors in both vascular remodelling and atherosclerosis progression. Interleukin-6 (IL-6) is an inflammatory cytokine with a key role in atherosclerosis. The relationship of osteoprotegerin, osteopontin, and IL-6 serum levels with endothelial function and arterial stiffness was evaluated in patients with coronary artery disease (CAD). Methods: We enrolled 219 patients with stable CAD and 112 control subjects. Osteoprotegerin, osteopontin and IL-6 serum levels were measured using an ELISA assay. Endothelial function was e

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Lindsey, Merry L., Fouad A. Zouein, Yuan Tian, Rugmani Padmanabhan Iyer, and Lisandra E. de Castro Brás. "Osteopontin is proteolytically processed by matrix metalloproteinase 9." Canadian Journal of Physiology and Pharmacology 93, no. 10 (2015): 879–86. http://dx.doi.org/10.1139/cjpp-2015-0019.

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Osteopontin is robustly upregulated following myocardial infarction (MI), which suggests that it has an important role in post-MI remodeling of the left ventricle (LV). Osteopontin deletion results in increased LV dilation and worsened cardiac function. Thus, osteopontin exerts protective effects post-MI, but the mechanisms have yet to be defined. Matrix metalloproteinases (MMPs) regulate LV remodeling post-MI, and osteopontin is a known substrate for MMP-2, -3, -7, and -9, although the cleavage sites have not been mapped. Osteopontin-derived peptides can exert distinct biological functions th

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Kuykindoll, R. J., H. Nishimura, D. B. Thomason, and S. K. Nishimoto. "Osteopontin expression in spontaneously developed neointima in fowl (Gallus gallus)." Journal of Experimental Biology 203, no. 2 (2000): 273–82. http://dx.doi.org/10.1242/jeb.203.2.273.

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Fowl show spontaneous elevation of blood pressure and neointimal plaque formation in the abdominal aorta at young ages. A similar neointima can be induced by a balloon-catheter-induced endothelium injury to the fowl aorta. Both spontaneously developed and injury-induced vascular lesions exhibit subendothelial hyperplasia consisting of neointimal cells with a synthetic phenotype and abundant extracellular matrix. The role of the extracellular matrix in the formation of neointima is not known. In this study, we investigated whether osteopontin, an adhesive glycoprotein present in the extracellul

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Hunter, G. K., C. L. Kyle, and H. A. Goldberg. "Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation." Biochemical Journal 300, no. 3 (1994): 723–28. http://dx.doi.org/10.1042/bj3000723.

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Osteopontin is a phosphorylated sialoprotein containing a conserved sequence of contiguous aspartic acid residues. This protein is expressed at high levels in mineralized tissues and has previously been shown to inhibit the in vitro formation of hydroxyapatite (HA). In the present study, protein modification and model compound studies have been used to identify the structural features of osteopontin that are responsible for its crystal-modulating properties. Using metastable calcium phosphate solutions buffered by autotitration, osteopontin caused half-maximal inhibition of HA formation at a c

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Rittling, Susan R., and David T. Denhardt. "Osteopontin Function in Pathology: Lessons from Osteopontin-Deficient Mice." Nephron Experimental Nephrology 7, no. 2 (1999): 103–13. http://dx.doi.org/10.1159/000020591.

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Lorenzen, Johan, Svjetlana Lovric, Robert Krämer, Hermann Haller, and Marion Haubitz. "Osteopontin in antineutrophil cytoplasmic autoantibody-associated vasculitis: relation to disease activity, organ manifestation and immunosuppressive therapy." Annals of the Rheumatic Diseases 69, no. 6 (2010): 1169–71. http://dx.doi.org/10.1136/ard.2009.113621.

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BackgroundOsteopontin is a pleiotropic cytokine involved in the recruitment and retention of neutrophils to sites of inflammation, which are the primary targets cells in antineutrophil cytoplasmic autoantibody-associated vasculitis (AAV). Osteopontin may play a role in the pathogenesis of AAV.Methods24 patients with systemic AAV and six patients with limited granulomatous disease were included. 19 patients were followed up at 6 and 12 months after the initiation of immunosuppressive therapy. 21 matched healthy volunteers and 20 body mass index and glomerular filtration rate-matched patients wi

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Boggio, Elena, Chiara Dianzani, Casimiro Luca Gigliotti, et al. "Thrombin Cleavage of Osteopontin Modulates Its Activities in Human CellsIn Vitroand Mouse Experimental Autoimmune EncephalomyelitisIn Vivo." Journal of Immunology Research 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/9345495.

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Osteopontin is a proinflammatory cytokine and plays a pathogenetic role in multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis (EAE), by recruiting autoreactive T cells into the central nervous system. Osteopontin functions are modulated by thrombin cleavage generating N- and C-terminal fragment, whose individual roles are only partly known. Published data are difficult to compare since they have been obtained with heterogeneous approaches. Interestingly, thrombin cleavage of osteopontin unmasks a cryptic domain of interaction withα4β1integrin that is the main ad

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Kars, T. U., M. Kulaksızoğlu, and İ. Kılınç. "Serum osteopontin can improve papillary thyroid cancer risk assessment of Bethesda III thyroid nodules: a preliminary study." Endocrine Oncology 1, no. 1 (2021): 17–22. http://dx.doi.org/10.1530/eo-21-0005.

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Objective Thyroid cancer can be detected in 5–10% of patients with thyroid nodules. Management may be a challenge if fine-needle aspiration biopsy yields Bethesda III findings. Most of these cases undergo surgery and are ultimately found benign. Our aim was to evaluate whether serum osteopontin can accurately estimate thyroid cancer risk in cases with cytologically Bethesda III thyroid nodules and, thereby, decrease the number of unnecessary surgical interventions. Design and Methods We obtained blood samples of cases with repeated cytologically Bethesda III thyroid nodules before surgery, and

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Albu (Matasariu), Daniela Roxana, Elena Mihalceanu, Alina Pangal, et al. "Can Osteopontin Be Considered a Biomarker for Endometriosis?" Revista de Chimie 68, no. 9 (2017): 2132–34. http://dx.doi.org/10.37358/rc.17.9.5840.

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Endometriosis is a multifactorial disease that is manifested by infertility and pelvic pain. The purpose of the study was to evaluate the effect of progesterone treatment on the serum level of osteopontin, a multipotent cytokine, in patients with endometriosis. The study was prospective and we evaluated osteopontin levels that were measured in the serum of 40 patients with endometriosis and 12 healthy women using a standardized Enzyme-Linked Immunosorbent Assay (ELISA) kit. Osteopontin seric levels were lower in endometriosis patients and increased after progesterone treatment. Because of the

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Zubareva, E. Yu, and M. A. Senchukova. "Prognostic and predictive significance of osteopontin in malignant neoplasms." Advances in Molecular Oncology 8, no. 2 (2021): 23–28. http://dx.doi.org/10.17650/2313-805x-2021-8-2-23-28.

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Osteopontin is an extracellular matrix protein which is produced by different types of cells and plays an important functional role in many biological processes. This review discusses the main functions of osteopontin, its role in the progression and chemoresistance of malignant neoplasms, in the regulation of epithelial-mesenchymal transition, angiogenesis, and the body’s immune response to the tumor. The article considers the currently known mechanisms by which osteopontin affects to the survival, mobility and invasion of tumor cells, to tumor sensitivity to drug treatment, as well as the pr

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CHEN, BO-LIN, GUI-YING ZHANG, SHI-PING WANG, et al. "The combined treatment of praziquantel with osteopontin immunoneutralization reduces liver damage in Schistosoma japonicum-infected mice." Parasitology 139, no. 4 (2012): 522–29. http://dx.doi.org/10.1017/s0031182011002241.

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SUMMARYThe aim of this study was to evaluate the therapeutic effects of osteopontin neutralization treatment on schistosome-induced liver injury in BALB/C mice. We randomly divided 100 BALB/C mice into groups A, B, C, D and group E. Mice in all groups except group A were abdominally infected with schistosomal cercariae to induce a schistosomal hepatopathological model. Mice in group C, D and group E were respectively administered with praziquantel, praziquantel plus colchicine and praziquantel plus neutralizing osteopontin antibody. We extracted mouse liver tissues at 3 and 9 weeks after the ‘

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Khalil, Ashraf, Jamalat Elgedawy, Mohammed F. Faramawi, et al. "Plasma Osteopontin Level as a Diagnostic Marker of Hepatocellular Carcinoma in Patients with Radiological Evidence of Focal Hepatic Lesions." Tumori Journal 99, no. 1 (2013): 100–107. http://dx.doi.org/10.1177/030089161309900117.

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Aims Hepatocellular carcinoma is one of the most aggressive malignant tumors and has limited treatment options. Needle-guided biopsies have been utilized as a tool to diagnose malignant focal hepatic lesions. These techniques are discouraged because of their complications. Nowadays, alpha fetoprotein is the most widely used tumor marker for screening and diagnosis of hepatocellular carcinoma. Nevertheless, this marker has limitations. The diagnostic role of plasma osteopontin as an adjuvant or alternative marker to alpha fetoprotein to detect hepatocellular carcinoma in Egyptian patients with

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Scatena, Marta, Manuela Almeida, Michelle L. Chaisson, Nelson Fausto, Roberto F. Nicosia та Cecilia M. Giachelli. "NF-κB Mediates αvβ3 Integrin-induced Endothelial Cell Survival". Journal of Cell Biology 141, № 4 (1998): 1083–93. http://dx.doi.org/10.1083/jcb.141.4.1083.

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The αvβ3 integrin plays a fundamental role during the angiogenesis process by inhibiting endothelial cell apoptosis. However, the mechanism of inhibition is unknown. In this report, we show that integrin-mediated cell survival involves regulation of nuclear factor-kappa B (NF-κB) activity. Different extracellular matrix molecules were able to protect rat aorta- derived endothelial cells from apoptosis induced by serum withdrawal. Osteopontin and β3 integrin ligation rapidly increased NF-κB activity as measured by gel shift and reporter activity. The p65 and p50 subunits were present in the shi

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Ge, Xiaodong, Yongke Lu, Tung-Ming Leung, Esben S. Sørensen, and Natalia Nieto. "Milk osteopontin, a nutritional approach to prevent alcohol-induced liver injury." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 10 (2013): G929—G939. http://dx.doi.org/10.1152/ajpgi.00014.2013.

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Alcohol consumption is a leading cause of liver disease worldwide; thus, there is an urgent need to develop novel therapeutic interventions. Key events for the onset and progression of alcoholic liver disease result in part from the gut-to-liver interaction. Osteopontin is a cytokine present at high concentration in human milk, umbilical cord, and infants' plasma with beneficial potential. We hypothesized that dietary administration of milk osteopontin could prevent alcohol-induced liver injury perhaps by maintaining gut integrity and averting hepatic inflammation and steatosis. Wild-type mice

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Gillezeau, Christina N., Maaike van Gerwen, Julio Ramos, Bian Liu, Raja Flores, and Emanuela Taioli. "Biomarkers for malignant pleural mesothelioma: a meta-analysis." Carcinogenesis 40, no. 11 (2019): 1320–31. http://dx.doi.org/10.1093/carcin/bgz103.

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Abstract Malignant pleural mesothelioma (MPM) is a rare but aggressive cancer, and early detection is associated with better survival. Mesothelin, fibulin-3 and osteopontin have been suggested as screening biomarkers. The study conducted a meta-analysis of the mean differences of mesothelin, osteopontin and fibulin-3 in blood and pleural samples. PubMed searches were conducted for studies that measured levels of mesothelin, osteopontin and fibulin-3 in participants with MPM compared with malignancy, benign lung disease or healthy participants. Thirty-two studies with mesothelin levels, 12 stud

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Hillerdal, Gunnar. "Mesothelin and osteopontin." European Respiratory Journal 42, no. 2 (2013): 557.1–557. http://dx.doi.org/10.1183/09031936.00052213.

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Pantazopoulos, Ioannis, Theodoros Xanthos, Paraskevi Boura, and Konstantinos Syrigos. "Mesothelin and osteopontin." European Respiratory Journal 42, no. 2 (2013): 557.2–558. http://dx.doi.org/10.1183/09031936.00064413.

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Salloum, Fadi N., and Vinh Q. Chau. "Osteopontin in HFpEF." Journal of the American College of Cardiology 73, no. 21 (2019): 2719–21. http://dx.doi.org/10.1016/j.jacc.2019.03.477.

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